We have developed a rapid, efficient, and reproducible method for the purification of thymosin α1 (Tα1) from thymosin fraction 5 (TF5). This procedure can serve as a model for isolation of other biologically active peptides from TF5 in sufficient quantity for characterization. The purification procedure is based on the use of high-performance preparative/semi-preparative and analytical reversed-phase (C18 Delta-Pak) chromatographic columns. The HPLC retention time, pI, RIA, SDS-PAGE, and amino acid composition analysis have shown that natural, purified Tα1 is identical to synthetic α1.
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Badamchian et al. (1989) studied this question.
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